| pubmed-article:1910046 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1910046 | lifeskim:mentions | umls-concept:C0598180 | lld:lifeskim |
| pubmed-article:1910046 | lifeskim:mentions | umls-concept:C0034818 | lld:lifeskim |
| pubmed-article:1910046 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
| pubmed-article:1910046 | lifeskim:mentions | umls-concept:C2003864 | lld:lifeskim |
| pubmed-article:1910046 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:1910046 | pubmed:dateCreated | 1991-10-21 | lld:pubmed |
| pubmed-article:1910046 | pubmed:abstractText | Biologically active colloid-gold complexes were used to compare ligand-induced microaggregation, redistribution, and internalization of insulin receptors on Rat 1 fibroblasts expressing wild type (HIRc) or tyrosine kinase-defective (HIR A/K1018) human insulin receptors. Insulin-like growth factor I (IGF I) and alpha 2-macroglobulin receptors also were compared. On both cell types, all four unoccupied receptor types occurred predominantly as single receptors. Ligand binding caused receptor microaggregation. Microaggregation of wild type or kinase-defective insulin receptors or IGF I receptors was not different. alpha 2-Macroglobulin receptors formed larger microaggregates. Compared to wild type insulin or IGF I receptors, accumulation of kinase-defective insulin receptor microaggregates in endocytic structures was decreased, and the size of microaggregates in coated pits was significantly smaller. As a result, receptor-mediated internalization of gold-insulin by HIR A/K1018 cells was less than 6% of the cell-associated particles compared to approximately 60% of the particles in HIRc cells. On HIR A/K1018 cells, alpha 2-macroglobulin and IGF I were internalized via coated pits demonstrating that those structures were functional. These results suggest that: 1) ATP binding, receptor autophosphorylation, and activation of receptor kinase activity are not required for receptor microaggregation; 2) receptor microaggregation per se is not sufficient to cause ligand-induced receptor-mediated internalization or the biological effects of insulin; and 3) autophosphorylation of the beta-subunit or activation of the receptor kinase activity is required for the insulin-induced concentration of occupied receptors in coated pits. | lld:pubmed |
| pubmed-article:1910046 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1910046 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1910046 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1910046 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1910046 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1910046 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1910046 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1910046 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1910046 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1910046 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1910046 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:1910046 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1910046 | pubmed:author | pubmed-author:SmithR MRM | lld:pubmed |
| pubmed-article:1910046 | pubmed:author | pubmed-author:JarettLL | lld:pubmed |
| pubmed-article:1910046 | pubmed:author | pubmed-author:OlefskyJ MJM | lld:pubmed |
| pubmed-article:1910046 | pubmed:author | pubmed-author:ShahNN | lld:pubmed |
| pubmed-article:1910046 | pubmed:author | pubmed-author:SeelyB LBL | lld:pubmed |
| pubmed-article:1910046 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1910046 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1910046 | pubmed:volume | 266 | lld:pubmed |
| pubmed-article:1910046 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1910046 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1910046 | pubmed:pagination | 17522-30 | lld:pubmed |
| pubmed-article:1910046 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:1910046 | pubmed:meshHeading | pubmed-meshheading:1910046-... | lld:pubmed |
| pubmed-article:1910046 | pubmed:meshHeading | pubmed-meshheading:1910046-... | lld:pubmed |
| pubmed-article:1910046 | pubmed:meshHeading | pubmed-meshheading:1910046-... | lld:pubmed |
| pubmed-article:1910046 | pubmed:meshHeading | pubmed-meshheading:1910046-... | lld:pubmed |
| pubmed-article:1910046 | pubmed:meshHeading | pubmed-meshheading:1910046-... | lld:pubmed |
| pubmed-article:1910046 | pubmed:meshHeading | pubmed-meshheading:1910046-... | lld:pubmed |
| pubmed-article:1910046 | pubmed:meshHeading | pubmed-meshheading:1910046-... | lld:pubmed |
| pubmed-article:1910046 | pubmed:meshHeading | pubmed-meshheading:1910046-... | lld:pubmed |
| pubmed-article:1910046 | pubmed:meshHeading | pubmed-meshheading:1910046-... | lld:pubmed |
| pubmed-article:1910046 | pubmed:meshHeading | pubmed-meshheading:1910046-... | lld:pubmed |
| pubmed-article:1910046 | pubmed:meshHeading | pubmed-meshheading:1910046-... | lld:pubmed |
| pubmed-article:1910046 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1910046 | pubmed:articleTitle | Tyrosine kinase-defective insulin receptors undergo insulin-induced microaggregation but do not concentrate in coated pits. | lld:pubmed |
| pubmed-article:1910046 | pubmed:affiliation | Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia 19104. | lld:pubmed |
| pubmed-article:1910046 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1910046 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1910046 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:1910046 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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